Sandbox313: Difference between revisions
| (6 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
'''This sandbox is in use until June 1, 2009 for UMass Chemistry 490a. Others please do not edit this page. Thanks!''' | |||
==Lipase (1lpm)== | ==Lipase (1lpm)== | ||
Mark Omobono, 03.02.09 | Mark Omobono, 03.02.09 | ||
{{STRUCTURE_1lpm | PDB=1lpm | SCENE= }} | |||
== About this enzyme == | |||
Lipase is a single-stranded enzyme that is responsible for breaking down the majority of the dietary lipids (triglycerides, fats, oils) digested by most living organisms. Lipases are located in the digestive juices and general digestive regions of an organism. They are also used in industry as yogurt and cheese fermentation vehicles, as well as more modern applications such as converting vegetable oil to usable fuel [http://en.wikipedia.org/wiki/Lipase]. | Lipase is a single-stranded enzyme that is responsible for breaking down the majority of the dietary lipids (triglycerides, fats, oils) digested by most living organisms. Lipases are located in the digestive juices and general digestive regions of an organism. They are also used in industry as yogurt and cheese fermentation vehicles, as well as more modern applications such as converting vegetable oil to usable fuel [http://en.wikipedia.org/wiki/Lipase]. | ||
Lipases catalyze the hydrolysis of ester bonds in lipids by employing a chymotrypsin-like hydrolysis mechanism. The enzyme itself is made up of both <scene name='Sandbox313/1lpmalphahelicies/2'>alpha</scene> and <scene name='Sandbox313/1lpmbetasheets/1'>beta</scene> | Lipases catalyze the hydrolysis of ester bonds in lipids by employing a chymotrypsin-like hydrolysis mechanism. The enzyme itself is made up of both <scene name='Sandbox313/1lpmalphahelicies/2'>alpha helicies</scene> and <scene name='Sandbox313/1lpmbetasheets/1'>beta sheets</scene>, but the enzyme activity hinges upon an alpha-beta hydrolase fold [http://en.wikipedia.org/wiki/Alpha/beta_hydrolase_fold]. Characteristics of this fold lie in a <scene name='Sandbox313/1lpmligand/2'>catalytic triad</scene>, all the pieces of which are located on loops.These include the reactive <scene name='Sandbox313/1lpmphosphane/1'>phosphonate</scene> center, two <scene name='Sandbox313/1lpmcalcium/1'>calcium ions</scene>, and two <scene name='Sandbox313/1lpmsugars/1'>sugars</scene> on the outside of the folded molecule. | ||
The molecule | The molecule contains many <scene name='Sandbox313/1lpmhydrophobic/3'>hydrophobic</scene> residues, but note that around the active phosphanate site (gold) there is a multitude of hydrophobic residues. This makes sense because the lipase enzyme catalyzes the hydrolysis of ''hydrophobic molecules'' as mentioned above. | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPM OCA]. | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LPM OCA]. | ||